The studies of substrate reaction mechanism mediated by Pseudomonas oleovorans and its ω-Hydroxylase

• Main Authors: Chih-Hsiang Chiang, 江志祥
• Other Authors: Sheng-Fa Yu
• Format: Others
• Language: zh-TW
• Published: 2007
• Online Access: http://ndltd.ncl.edu.tw/handle/7qh3eg

碩士 === 國立東華大學 === 生物技術研究所 === 95 === The non-heme diiron monooxygenase, alkane hydroxylase (alkB) from Pseudomonas olevorans is an integral membrance protein which can catalyzes the terminal methyl group hydroxylation of alkane. Medium-chain-length alkane(C5 to C12 alkanes) and terminal olefins can also be oxidized to the corresponding alcohols or epoxides by this enzyme. This oxidation also contain two soluble proteins (named rubredoxin [AlkG] and rubredoxin reductase [AlkT]). Rubredoxin reductases transfer the electrons from NADH to rubredoxin, which in turn transfer the electrons to the membrane-bound alkane hydroxylase [AlkB]. AlkB transfers one oxygen atom from O2 to one of the terminal methyl groups of the alkane molecule, rendering an alcohol, while the other oxygen atom is reduced to H2O by the electron transfer mediated through rubredoxin. To understand the uniqueness of floriated octane activity by ω-hydroxylase synthesize perfluoro octane derivatives by microwave assisted reaction method. The chemical conversion process be carried out with a substantial reduction in the reaction time in comparison to conventional processes. Towards to the end, we found that alkB can oxidize the terminal methyl group of 2,2-difluorooctane and 3,3-difluorooctane to obtain 7,7-difluorooctanoic acid and 6,6-difluorooctanoic acid, respectively. The C-F bond has unusual hydrophobic property, so that fluorinated octane can affinity with